9LU9

The chimeric flagellar motor complex between MotA1B1 from Paenibacillus sp. TCA20 and MotAB from E.coli, state 1

9LU9 の概要

• エントリーDOI: 10.2210/pdb9lu9/pdb
• EMDBエントリー: 63392
• 分子名称: Flagellar motor protein MotA, MotB1,Motility protein B, Lauryl Maltose Neopentyl Glycol (3 entities in total)
• 機能のキーワード: flagellar, motility, paenibacillus, motor protein
• 由来する生物種: Paenibacillus sp. TCA20; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 214370.88

構造登録者

Onoe, S.,Nishikino, T.,Kinoshita, M.,Kishikawa, J.,Kato, T. (登録日: 2025-02-08, 公開日: 2025-04-09)

主引用文献

Onoe, S.,Nishikino, T.,Kinoshita, M.,Takekawa, N.,Minamino, T.,Imada, K.,Namba, K.,Kishikawa, J.I.,Kato, T.
Cryo-EM Structure of the Flagellar Motor Complex from Paenibacillus sp. TCA20.
Biomolecules, 15:-, 2025

PubMed Abstract: The bacterial flagellum, a complex nanomachine composed of numerous proteins, is utilized by bacteria for swimming in various environments and plays a crucial role in their survival and infection. The flagellar motor is composed of a rotor and stator complexes, with each stator unit functioning as an ion channel that converts flow from outside of cell membrane into rotational motion. sp. TCA20 was discovered in a hot spring, and a structural analysis was conducted on the stator complex using cryo-electron microscopy to elucidate its function. Two of the three structures (Classes 1 and 3) were found to have structural properties typical for other stator complexes. In contrast, in Class 2 structures, the pentamer ring of the A subunits forms a C-shape, with lauryl maltose neopentyl glycol (LMNG) bound to the periplasmic side of the interface between the A and B subunits. This interface is conserved in all stator complexes, suggesting that hydrophobic ligands and lipids can bind to this interface, a feature that could potentially be utilized in the development of novel antibiotics aimed at regulating cell motility and infection.

PubMed: 40149971
DOI: 10.3390/biom15030435

実験手法

ELECTRON MICROSCOPY (3.3 Å)